ID   A16_VACCC               Reviewed;         378 AA.
AC   P20993;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Virion membrane protein A16;
GN   ORFNames=A16L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
RN   [3]
RP   MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2.
RX   PubMed=9188589; DOI=10.1128/jvi.71.7.5218-5226.1997;
RA   Martin K.H., Grosenbach D.W., Franke C.A., Hruby D.E.;
RT   "Identification and analysis of three myristylated vaccinia virus late
RT   proteins.";
RL   J. Virol. 71:5218-5226(1997).
CC   -!- FUNCTION: Envelope protein part of the entry-fusion complex responsible
CC       for the virus membrane fusion with host cell membrane during virus
CC       entry. Also plays a role in cell-cell fusion (syncytium formation) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a stable entry-fusion complex (EFC) which is at least
CC       composed of proteins A16, A21, A28, G3, G9, H2, J5, and L5. Formation
CC       of the viral membrane is necessary for the assembly of the complex.
CC       Interacts with G9 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC       II membrane protein {ECO:0000305}. Note=Component of the mature virion
CC       (MV) membrane. The mature virion is located in the cytoplasm of
CC       infected cells and is probably released by cell lysis. {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- PTM: Most cysteines are linked by disulfide bonds. They are created by
CC       the viral disulfide bond formation pathway, a poxvirus-specific redox
CC       pathway that operates on the cytoplasmic side of the MV membranes (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the poxviridae A16/G9/J5 family. {ECO:0000305}.
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DR   EMBL; M35027; AAA48138.1; -; Genomic_DNA.
DR   PIR; I42518; I42518.
DR   SMR; P20993; -.
DR   iPTMnet; P20993; -.
DR   Proteomes; UP000008269; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR004251; Pox_virus_G9/A16.
DR   Pfam; PF03003; Pox_G9-A16; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Fusion of virus membrane with host membrane; Late protein;
KW   Lipoprotein; Membrane; Myristate; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT   CHAIN           2..378
FT                   /note="Virion membrane protein A16"
FT                   /id="PRO_0000099251"
FT   TOPO_DOM        2..342
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..378
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000269|PubMed:9188589"
FT   MUTAGEN         2
FT                   /note="G->A: Complete loss of myristoylation."
FT                   /evidence="ECO:0000269|PubMed:9188589"
SQ   SEQUENCE   378 AA;  43562 MW;  05ED614AA1D11A19 CRC64;
     MGAAVTLNRI KIAPGIADIR DKYMELGFNY PEYNRAVKFA EESYTYYYET SPGEIKPKFC
     LIDGMSIDHC SSFIVPEFAK QYVLIHGEPC SSFKFRPGSL IYYQNEVTPE YIKDLKHATD
     YIASGQRCHF IKKDYLLGDS DSVAKCCSKT NTKHCPKIFN NNYKTEHCDD FMTGFCRNDP
     GNPNCLEWLR AKRKPAMSTY SDICSKHMDA RYCSEFIRII RPDYFTFGDT ALYVFCNDHK
     GNRNCWCANY PKSNSGDKYL GPRVCWLHEC TDESRDRKWL YYNQDVQRTR CKYVGCTINV
     NSLALKNSQA ELTSNCTRTT SAVGDVHHPG EPVVKDKIKL PTWLGAAITL VVISVIFYFI
     SIYSRPKIKT NDINVRRR